Puohiniemi R, Muotiala A, Helander I M, Sarvas M
Department of Molecular Bacteriology, National Public Health Institute, Helsinki, Finland.
FEMS Microbiol Lett. 1993 Jan 1;106(1):105-10. doi: 10.1111/j.1574-6968.1993.tb05942.x.
The conformation of the outer membrane protein OmpA of Escherichia coli produced in Bacillus subtilis and solubilized in Sarkosyl was studied by measuring its ability to bind OmpA-specific phage K3 and to inhibit F-mediated conjugation. The partially purified protein was inactive in both of these assays. Refolding of the protein in the presence of lipopolysaccharide resulted in preparations with full phage-binding and conjugation-inhibiting capacity, indicating the formation of surface-exposed loops of OmpA of native conformation. The finding is of importance for the potential use of outer membrane proteins of Gram-negative bacteria as vaccines.
通过测量在枯草芽孢杆菌中产生并溶于十二烷基肌氨酸钠的大肠杆菌外膜蛋白OmpA结合OmpA特异性噬菌体K3的能力以及抑制F介导的接合的能力，对其构象进行了研究。部分纯化的蛋白在这两种测定中均无活性。在脂多糖存在下对该蛋白进行重折叠，得到的制剂具有完全的噬菌体结合和接合抑制能力，表明形成了天然构象的OmpA表面暴露环。这一发现对于革兰氏阴性菌外膜蛋白作为疫苗的潜在用途具有重要意义。
